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Structure of phosphomonoesterase

Analyse Structure of phosphomonoesterase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IHP
Type: protein
Length: 434 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phytase
EC: 3.1.3.8
UniProt: P34752
Ligands: SO4
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phytase (EC 3.1.3.8)	protein	434	44% helix, 13% strand	P34752

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	323	0.55	0.75	38	empty
2	112	0.44	0.77	20	empty
3	53	0.27	0.74	21	empty

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

1IHP · Structure of phosphomonoesterase · the same entry in another collection · chain A against A, TM-score 1.00
P34752 · AlphaFold monomer V2.0 prediction for 3-phytase a (P34752) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P34752
Elsewhere: RCSB PDB 1IHP · PDBe 1IHP · UniProt P34752

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